2006
Regulation of Cell Adhesion Responses by Abl Family Kinases
Tanis K, Schwartz M. Regulation of Cell Adhesion Responses by Abl Family Kinases. Molecular Biology Intelligence Unit 2006, 16-25. DOI: 10.1007/978-0-387-68744-5_3.Peer-Reviewed Original ResearchAbl family kinasesFamily kinasesAbl familyMultiple focal adhesion proteinsFocal adhesion proteinsCytoskeletal regulatory proteinsNonreceptor tyrosine kinaseCell cycle progressionCell surface receptorsCell adhesive responsesInteraction of cellsIntegrin engagementRegulatory proteinsAdhesion proteinsGene expressionCell adhesion responsesCycle progressionCell spreadingTyrosine kinaseCellular responsesHuman diseasesCell survivalNuclear processesKinaseExtracellular matrix
2003
Modulation of DNA damage-induced apoptosis by cell adhesion is independently mediated by p53 and c-Abl
Truong T, Sun G, Doorly M, Wang JY, Schwartz MA. Modulation of DNA damage-induced apoptosis by cell adhesion is independently mediated by p53 and c-Abl. Proceedings Of The National Academy Of Sciences Of The United States Of America 2003, 100: 10281-10286. PMID: 12928501, PMCID: PMC193552, DOI: 10.1073/pnas.1635435100.Peer-Reviewed Original ResearchConceptsC-Abl/p73 pathwayDNA damageIntegrin ligationC-AblDNA damage-induced apoptosisC-Abl tyrosine kinaseCell adhesionExtracellular matrixDamage-induced apoptosisP73 pathwayCertain cell typesP53-negative tumor cellsProapoptotic transcription factorTranscription factorsTyrosine kinaseApoptotic responseDifferential utilizationCell typesDifferent tumor cell linesTumor cell linesTumor cellsP53 levelsCell linesSecond pathwayCell killing
2001
Coordinate signaling by integrins and receptor tyrosine kinases in the regulation of G1 phase cell-cycle progression
Assoian R, Schwartz M. Coordinate signaling by integrins and receptor tyrosine kinases in the regulation of G1 phase cell-cycle progression. Current Opinion In Genetics & Development 2001, 11: 48-53. PMID: 11163150, DOI: 10.1016/s0959-437x(00)00155-6.Peer-Reviewed Original ResearchConceptsCell cycle progressionReceptor tyrosine kinasesG1 phase cyclinsDependent kinasesTyrosine kinasePhase cell cycle progressionG1 phase cell cycle progressionExtracellular matrix proteinsSoluble growth factorsRho GTPasesGrowth factor receptorRegulated signalingMatrix proteinsKinaseG1 phaseCell proliferationIntegrinsCyclinGrowth factorRecent studiesGTPasesActivationReceptorsSignalingERK
2000
The Molecular Adapter SLP-76 Relays Signals from Platelet Integrin αIIbβ3 to the Actin Cytoskeleton*
Obergfell A, Judd B, del Pozo M, Schwartz M, Koretzky G, Shattil S. The Molecular Adapter SLP-76 Relays Signals from Platelet Integrin αIIbβ3 to the Actin Cytoskeleton*. Journal Of Biological Chemistry 2000, 276: 5916-5923. PMID: 11113155, DOI: 10.1074/jbc.m010639200.Peer-Reviewed Original ResearchMeSH KeywordsActinsAdaptor Proteins, Signal TransducingAnimalsBlood PlateletsCell AdhesionCell Cycle ProteinsCHO CellsCricetinaeCytoskeletonEnzyme PrecursorsFibrinogenHumansIntracellular Signaling Peptides and ProteinsPhosphoproteinsPhosphorylationPlatelet Glycoprotein GPIIb-IIIa ComplexProtein BindingProtein-Tyrosine KinasesProto-Oncogene ProteinsProto-Oncogene Proteins c-vavPseudopodiaRac GTP-Binding ProteinsSignal TransductionSyk KinaseConceptsSLP-76SLAP-130Lamellipodia formationSLP-76 functionAdhesion-dependent activationCHO cell adhesionCell expression systemSLP-76 phosphorylationChinese hamster ovary cell expression systemSLP-76 expressionSyk tyrosine kinasePlatelet integrin αIIbβ3Sites of adhesionRac effectorPAK kinasesActin cytoskeletonAdherent CHO cellsExchange factorActin rearrangementCytoskeletal reorganizationActin reorganizationTyrosine phosphorylationExpression systemCell spreadingTyrosine kinaseThe c-Abl tyrosine kinase contributes to the transient activation of MAP kinase in cells plated on fibronectin
Renshaw M, Lewis J, Schwartz M. The c-Abl tyrosine kinase contributes to the transient activation of MAP kinase in cells plated on fibronectin. Oncogene 2000, 19: 3216-3219. PMID: 10918577, DOI: 10.1038/sj.onc.1203667.Peer-Reviewed Original ResearchMeSH Keywords3T3 CellsAdaptor Proteins, Signal TransducingAnimalsCell Culture TechniquesEnzyme ActivationFibronectinsFocal Adhesion Kinase 1Focal Adhesion Protein-Tyrosine KinasesGRB2 Adaptor ProteinMAP Kinase Signaling SystemMiceMitogen-Activated Protein Kinase 1Mitogen-Activated Protein KinasesProtein-Tyrosine KinasesProteinsProto-Oncogene Proteins c-abl
1998
Integrins Regulate the Association and Phosphorylation of Paxillin by c-Abl*
Lewis J, Schwartz M. Integrins Regulate the Association and Phosphorylation of Paxillin by c-Abl*. Journal Of Biological Chemistry 1998, 273: 14225-14230. PMID: 9603926, DOI: 10.1074/jbc.273.23.14225.Peer-Reviewed Original ResearchConceptsC-AblCell adhesionTyrosine kinaseFocal adhesion protein paxillinNon-receptor tyrosine kinasePhosphorylation of paxillinC-Abl kinaseEffects of integrinsFocal adhesionsProtein paxillinIntegrin regulationPaxillinTransient recruitmentKinaseIntegrinsCell functionProteinAdhesionPhosphorylationTyrosineRegulationABLRecruitmentActivationLocalization
1996
Integrin regulation of c-Abl tyrosine kinase activity and cytoplasmic–nuclear transport
Lewis J, Baskaran R, Taagepera S, Schwartz M, Wang J. Integrin regulation of c-Abl tyrosine kinase activity and cytoplasmic–nuclear transport. Proceedings Of The National Academy Of Sciences Of The United States Of America 1996, 93: 15174-15179. PMID: 8986783, PMCID: PMC26376, DOI: 10.1073/pnas.93.26.15174.Peer-Reviewed Original ResearchConceptsNuclear c-AblC-AblKinase activityC-Abl tyrosine kinase activityTyrosine kinaseCell adhesionCell cycle signalsCytoplasmic-nuclear transportExtracellular matrix protein fibronectinNonreceptor tyrosine kinaseCytoplasmic c-AblC-Abl activationC-Abl activityMatrix protein fibronectinTyrosine kinase activityC-abl protooncogeneMin of adhesionIntegrin regulationSubcellular localizationIntegrin signalsFocal contactsCytoplasmic poolTransient recruitmentSubcellular distributionProtein fibronectin
1995
Integrin signaling: roles for the cytoplasmic tails of αIIbβ3 in the tyrosine phosphorylation of pp125FAK
Leong L, Hughes P, Schwartz M, Ginsberg M, Shattil S. Integrin signaling: roles for the cytoplasmic tails of αIIbβ3 in the tyrosine phosphorylation of pp125FAK. Journal Of Cell Science 1995, 108: 3817-3825. PMID: 8719888, DOI: 10.1242/jcs.108.12.3817.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsCell Adhesion MoleculesCHO CellsCricetinaeCytoplasmEnzyme ActivationFocal Adhesion Kinase 1Focal Adhesion Protein-Tyrosine KinasesMolecular Sequence DataMutagenesisPhosphorylationPlatelet Glycoprotein GPIIb-IIIa ComplexProtein-Tyrosine KinasesSignal TransductionConceptsAlpha IIbCytoplasmic tailTruncation mutantsFAK phosphorylationCytoplasmic tail truncation mutantsMembrane-proximal portionProtein tyrosine kinasesMembrane-distal portionExtent of phosphorylationLatter mutantTyrosine phosphorylationPersistent phosphorylationCell spreadingMutantsTyrosine kinaseCellular responsesExtracellular portionPhosphorylationCell adhesionFAKAdhesive ligandsCHO cellsPp125FAKAdditional mutationsBeta 3